Jakob U, Buchner J
Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.
Trends Biochem Sci. 1994 May;19(5):205-11. doi: 10.1016/0968-0004(94)90023-x.
Hsp90 and small Hsps are two abundant types of eukaryotic stress protein whose function has remained largely enigmatic. In the cell, Hsp90 exists in a complex (with other Hsps and prolyl isomerases) possibly implicated in interactions with non-native proteins. Recent biochemical analysis of both Hsp90 and small Hsps has revealed that they may act as ATP-independent molecular chaperones involved in protein folding and unfolding events.
热休克蛋白90（Hsp90）和小分子热休克蛋白（small Hsps）是真核生物中两种丰富的应激蛋白类型，其功能在很大程度上仍然是个谜。在细胞中，Hsp90以一种复合物的形式存在（与其他热休克蛋白和脯氨酰异构酶一起），可能参与与非天然蛋白质的相互作用。最近对Hsp90和小分子热休克蛋白的生化分析表明，它们可能作为不依赖ATP的分子伴侣参与蛋白质的折叠和去折叠过程。
